2-(3-Amino-3-Carboxypropyl)histidine Synthase Subunit 1 (DPH1) Antibody

Background

DPH1 is a key enzyme involved in the biosynthesis of diphthamide, a unique post-translational modification of histidine residue found exclusively on eukaryotic elongation factor 2 (eEF2). This modification is critical for cellular protein synthesis and is targeted by bacterial toxins such as diphtheria toxin and Pseudomonas exotoxin A. DPH1 functions as part of a complex multiprotein pathway that catalyzes the initial step of diphthamide synthesis, converting a specific histidine residue on eEF2 into an intermediate form. Genetic mutations or deletions in DPH1 have been implicated in various human diseases, including developmental disorders and cancer. DPH1's role extends beyond diphthamide biosynthesis, with studies suggesting its involvement in embryonic development, particularly neural tube closure, and hematopoiesis. Structurally, DPH1 contains conserved domains required for its catalytic activity and interactions with other diphthamide biosynthesis proteins like DPH2 and DPH3. Loss of DPH1 function impairs cellular sensitivity to diphtheria toxin, providing a functional assay for its activity. DPH1 is ubiquitously expressed, with the highest levels found in actively proliferating tissues. It also exhibits a conserved role in diphthamide synthesis across eukaryotes, underscoring its evolutionary significance.